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Gross, H.* ; Hennard, C. ; Masouris, I. ; Cassel, C.* ; Barth, S.* ; Stober-Grässer, U.* ; Mamiani, A.* ; Moritz, B.* ; Ostareck, D.* ; Ostareck-Lederer, A.* ; Neuenkirchen, N.* ; Fischer, U.* ; Deng, W.* ; Leonhardt, H.* ; Nößner, E. ; Kremmer, E. ; Grässer, F.A.*

Binding of the heterogeneous ribonucleoprotein K (hnRNP K) to the Epstein-Barr virus nuclear antigen 2 (EBNA2) enhances viral LMP2A expression.

PLoS ONE 7:e42106 (2012)

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The Epstein-Barr Virus (EBV) -encoded EBNA2 protein, which is essential for the in vitro transformation of B-lymphocytes, interferes with cellular processes by binding to proteins via conserved sequence motifs. Its Arginine-Glycine (RG) repeat element contains either symmetrically or asymmetrically di-methylated arginine residues (SDMA and ADMA, respectively). EBNA2 binds via its SDMA-modified RG-repeat to the survival motor neurons protein (SMN) and via the ADMA-RG-repeat to the NP9 protein of the human endogenous retrovirus K (HERV-K (HML-2) Type 1). The hypothesis of this work was that the methylated RG-repeat mimics an epitope shared with cellular proteins that is used for interaction with target structures. With monoclonal antibodies against the modified RG-repeat, we indeed identified cellular homologues that apparently have the same surface structure as methylated EBNA2. With the SDMA-specific antibodies, we precipitated the Sm protein D3 (SmD3) which, like EBNA2, binds via its SDMA-modified RG-repeat to SMN. With the ADMA-specific antibodies, we precipitated the heterogeneous ribonucleoprotein K (hnRNP K). Specific binding of the ADMA-antibody to hnRNP K was demonstrated using E. coli expressed/ADMA-methylated hnRNP K. In addition, we show that EBNA2 and hnRNP K form a complex in EBV-infected B-cells. Finally, hnRNP K, when co-expressed with EBNA2, strongly enhances viral latent membrane protein 2A (LMP2A) expression by an unknown mechanism as we did not detect a direct association of hnRNP K with DNA-bound EBNA2 in gel shift experiments. Our data support the notion that the methylated surface of EBNA2 mimics the surface structure of cellular proteins to interfere with or co-opt their functional properties.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords PROTEIN ARGININE METHYLTRANSFERASE; MOTOR-NEURON PROTEIN; RNA-POLYMERASE-II; MESSENGER-RNA; C-MYC; GENE-EXPRESSION; SPLICING FACTOR; DOWN-REGULATION; LIVING CELLS; SM PROTEINS

ISSN (print) / ISBN 1932-6203

Journal PLoS ONE

Quellenangaben Volume: 7, Issue: 8, Article Number: e42106

Publisher Public Library of Science (PLoS)

Publishing Place Lawrence, Kan.

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Molecular Immunology (IMI)